title: Spermine binding to liver mitochondria deenergized by ruthenium red plus either FCCP or antimycin A.
abstract: Thermodynamic analysis of spermine binding to mitochondria treated with ruthenium red and deenergized with either FCCP or antimycin A confirms the presence of two polyamine binding sites, S1 and S2, both with monocoordination, as previously observed in energized mitochondria [Dalla Via et al., Biochim. Biophys. Acta 1284 (1996) 247-252]. Both sites undergo a marked change in binding capacity and binding affinity upon mitochondrial deenergization. This change is most likely responsible for the incomplete or delayed spermine-mediated inhibition of the permeability transition induced in deenergized mitochondria.
authors.affiliation: Dipartimento di Scienze Farmaceutiche, Università di Padova, Padua, Italy.
authors.forename: L
authors.initials: L
authors.lastname: Dalla Via
authors.forename: V
authors.initials: V
authors.lastname: Di Noto
authors.forename: A
authors.initials: A
authors.lastname: Toninello
mesh_terms: D000818:Animals; D000968:Antimycin A / Q000494:pharmacology*; D001665:Binding Sites; D002259:Carbonyl Cyanide p-Trifluoromethoxyphenylhydrazone / Q000494:pharmacology*; D004734:Energy Metabolism / Q000187:drug effects; D008930:Mitochondria, Liver / Q000187:drug effects* / Q000378:metabolism; D008933:Mitochondrial Swelling / Q000187:drug effects; D011485:Protein Binding / Q000187:drug effects; D051381:Rats; D012430:Ruthenium Red / Q000494:pharmacology; D013096:Spermine / Q000378:metabolism*; D013816:Thermodynamics
chemical_list: D012430:Ruthenium Red; D013096:Spermine; D002259:Carbonyl Cyanide p-Trifluoromethoxyphenylhydrazone; D000968:Antimycin A